6533b854fe1ef96bd12af546

RESEARCH PRODUCT

Bioavailability of antihypertensive lactoferricin B-derived peptides: Transepithelial transport and resistance to intestinal and plasma peptidases

Ricardo Fernández-musolesIsidra RecioMaría Del Mar ContrerasMaría Castelló-ruizPaloma ManzanaresJuan B. Salom

subject

chemistry.chemical_classificationPeptideAbsorption (skin)Applied Microbiology and BiotechnologyBioavailabilitychemistry.chemical_compoundEnzymechemistryBiochemistryIntestinal mucosaLactoferricinParacellular transportRenin–angiotensin systemFood Science

description

The transepithelial transport of the angiotensin I-converting enzyme (ACE)-inhibitory and antihypertensive lactoferricin B (LfcinB)-derived hexapeptide LfcinB20-25 (RRWQWR) and of its two main fragments RWQ and WQ were investigated using a human intestinal cell (Caco-2) monolayer. The three peptides were susceptible to the action of brush-border peptidases. Intact LfcinB20-25 was not transported across Caco-2 whereas RWQ and WQ were both absorbed through the cell monolayer. Apparent permeability (Papp) values for absorptive transport across the monolayer were 0.7×10-8cms-1 (RWQ) and 3.9×10-8cms-1 (WQ). The effect of pathway-selective inhibitors on peptide absorption suggested paracellular diffusion as the main mechanism for the transport of intact RWQ and WQ. Invitro incubation in human plasma showed half-life values of 1.9min (RWQ) and 2.3h (WQ). These results highlight the possibility of transport of antihypertensive lactoferricin B-derived peptides across human intestinal mucosa. © 2013 Elsevier Ltd.

yearjournalcountryeditionlanguage
2013-10-01
http://hdl.handle.net/10261/99815